Stability of proteins inside a hydrophobic cavity

Langmuir

Volumn 29, Issue 28, 2013, Pages 8922-8928

  Radhakrishna, Mithun ^a   Grimaldi, Joseph ^b   Belfort, Georges ^b   Kumar, Sanat K ^a  

^a Department of Earth and Environmental Sciences   (United States)

^b Rensselaer Polytechnic Institute   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; ENZYME PERFORMANCE; HYDROPHILIC AND HYDROPHOBIC; HYDROPHOBIC CAVITIES; HYDROPHOBIC CONFINEMENT; PROTEIN-SURFACE INTERACTIONS; SPHERICAL CAVITIES; SURFACE HYDROPHOBICITY;

ENTROPY; ENZYMES; HYDROPHILICITY; PROTEINS;

HYDROPHOBICITY;

ALCOHOL DEHYDROGENASE; METHACRYLIC ACID; METHACRYLIC ACID DERIVATIVE; PROTEIN; SBA 15; SBA-15; SILICON DIOXIDE;

ARTICLE; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; POROSITY; PROTEIN CONFORMATION; PROTEIN STABILITY; SURFACE PROPERTY;

ALCOHOL DEHYDROGENASE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; METHACRYLATES; MODELS, MOLECULAR; POROSITY; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEINS; SILICON DIOXIDE; SURFACE PROPERTIES;

EID: 84880263124     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la4014784     Document Type: Article

References (41)

1. Hartl, F. U.; Bracher, A.; Hayer-Hartl, M. Molecular chaperones in protein folding and proteostasis Nature 2011, 475 (7356) 324-332
2. Jin, W.; Brennan, J. D. Properties and applications of proteins encapsulated within sol-gel derived materials Anal. Chim. Acta 2002, 461 (1) 1-36
3. Andrews, T. M.; Tata, J. R. Protein synthesis by membrane-bound and free ribosomes of secretory and non-secretory tissues Biochem. J. 1971, 121 (4) 683-694
4. Martin, J.; Langer, T.; Boteva, R.; Schramel, A.; Horwich, A. L.; Hartl, F. U. Chaperonin-mediated protein folding at the surface of groEL through a "molten globule"-like intermediate Nature 1991, 352 (6330) 36-42
5. Zimmerman, S. B.; Minton, A. P. Macromolecular crowding-Biochemical, biophysical, and physiological consequences Annu. Rev. Biophys. Biomol. Struct. 1993, 22, 27-65
6. Ellis, R. J. Macromolecular crowding: Obvious but underappreciated Trends Biochem. Sci. 2001, 26 (10) 597-604
7. Ellis, R. J.; Minton, A. P. Cell biology-Join the crowd Nature 2003, 425 (6953) 27-28
8. Kirschner, D. A.; Abraham, C.; Selkoe, D. J. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation Proc. Natl. Acad. Sci. U.S.A. 1986, 83 (2) 503-507
9. Conway, K. A.; Lee, S. J.; Rochet, J. C.; Ding, T. T.; Williamson, R. E.; Lansbury, P. T. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy Proc. Natl. Acad. Sci. U.S.A. 2000, 97 (2) 571-576
10. Koo, E. H.; Lansbury, P. T.; Kelly, J. W. Amyloid diseases: Abnormal protein aggregation in neurodegeneration Proc. Natl. Acad. Sci. U.S.A. 1999, 96 (18) 9989-9990
11. Kelly, J. W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways Curr. Opin. Struct. Biol. 1998, 8 (1) 101-106
12. Jewett, A. I.; Shea, J. E. Folding on the chaperone: Yield enhancement through loose binding J. Mol. Biol. 2006, 363 (5) 945-957
13. Corrales, F. J.; Fersht, A. R. Toward a mechanism for GroEL center dot GroES chaperone activity: An ATPase-gated and -pulsed folding and annealing cage Proc. Natl. Acad. Sci. U.S.A. 1996, 93 (9) 4509-4512
14. Eggers, D. K.; Valentine, J. S. Molecular confinement influences protein structure and enhances thermal protein stability Protein Sci. 2001, 10 (2) 250-261
15. Sheldon, R. A. Enzyme immobilization: The quest for optimum performance Adv. Synth. Catal. 2007, 349 (8-9) 1289-1307
16. Wang, Y. J.; Caruso, F. Mesoporous silica spheres as supports for enzyme immobilization and encapsulation Chem. Mater. 2005, 17 (5) 953-961
17. Zhou, H. X.; Dill, K. A. Stabilization of proteins in confined spaces Biochemistry 2001, 40 (38) 11289-11293
18. Rathore, N.; Knotts, T. A.; de Pablo, J. J. Confinement effects on the thermodynamics of protein folding: Monte Carlo simulations Biophys. J. 2006, 90 (5) 1767-1773
19. Andrade, J. D.; Hlady, V. Protein adsorption and materials biocompatibility-A tutorial review and suggested hypotheses Adv. Polym. Sci. 1986, 79, 1-63
20. Vermeer, A. W. P.; Giacomelli, C. E.; Norde, W. Adsorption of IgG onto hydrophobic Teflon. Differences between the Fab and Fc domains Biochim. Biophys. Acta, Gen. Subj. 2001, 1526 (1) 61-69
21. Norde, W.; Favier, J. P. Structure of adsorbed and desorbed proteins Colloids Surf. 1992, 64 (1) 87-93
22. Haynes, C. A.; Norde, W. Globular proteins at solid/liquid interfaces Colloids Surf., B 1994, 2 (6) 517-566
23. Felsovalyi, F.; Mangiagalli, P.; Bureau, C.; Kumar, S. K.; Banta, S. Reversibility of the adsorption of lysozyme on silica Langmuir 2011, 27 (19) 11873-11882
24. Raffaini, G.; Ganazzoli, F. Protein adsorption on a hydrophobic surface: A molecular dynamics study of lysozyme on graphite Langmuir 2010, 26 (8) 5679-5689
25. Sharma, S.; Berne, B. J.; Kumar, S. K. Thermal and structural stability of adsorbed proteins Biophys. J. 2010, 99 (4) 1157-1165
26. Sang, L. C.; Coppens, M. O. Effects of surface curvature and surface chemistry on the structure and activity of proteins adsorbed in nanopores Phys. Chem. Chem. Phys. 2011, 13 (14) 6689-6698
27. Dill, K. A. Theory for the folding and stability of globular proteins Biochemistry 1985, 24 (6) 1501-1509
28. Yue, K.; Dill, K. A. Forces of tertiary structural organization in globular proteins Proc. Natl. Acad. Sci. U.S.A. 1995, 92 (1) 146-150
29. Yue, K.; Fiebig, K. M.; Thomas, P. D.; Chan, H. S.; Shakhnovich, E. I.; Dill, K. A. A test of lattice protein-folding algorithms Proc. Natl. Acad. Sci. U.S.A. 1995, 92 (1) 325-329
30. Berger, B.; Leighton, T. Protein folding in the hydrophobic-hydrophilic (HP) model is NP-complete J. Comput. Biol. 1998, 5 (1) 27-40
31. Crescenzi, P.; Goldman, D.; Papadimitriou, C.; Piccolboni, A.; Yannakakis, M. On the complexity of protein folding J. Comput. Biol. 1998, 5 (3) 423-465
32. Metropolis, N.; Rosenbluth, A. W.; Rosenbluth, M. N.; Teller, A. H.; Teller, E. Equation of state calculations by fast computing machines J. Chem. Phys. 1953, 21 (6) 1087-1092
33. Wood, W. W.; Jacobson, J. D. Preliminary results from a recalculation of the Monte Carlo equation of state of hard spheres J. Chem. Phys. 1957, 27 (5) 1207-1208
34. Siepmann, J. I.; Frenkel, D. configurational bias Monte Carlo-A new sampling scheme for flexible chains Mol. Phys. 1992, 75 (1) 59-70
35. Ferrenberg, A. M.; Swendsen, R. H. Optimized Monte Carlo data analysis Phys. Rev. Lett. 1989, 63 (12) 1195-1198
36. Kumar, S.; Bouzida, D.; Swendsen, R. H.; Kollman, P. A.; Rosenberg, J. M. The weighted histogram analysis method for free-energy calculations on biomolecules. 1. The method J. Comput. Chem. 1992, 13 (8) 1011-1021
37. Zhou, H. X.; Rivas, G. N.; Minton, A. P. Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences Annu. Rev. Biophys. 2008, 37, 375-397
38. Friedel, M.; Sheeler, D. J.; Shea, J. E. Effects of confinement and crowding on the thermodynamics and kinetics of folding of a minimalist beta-barrel protein J. Chem. Phys. 2003, 118 (17) 8106-8113
39. Wang, G.; Yau, S. T. Spatial confinement induced enzyme stability for bioelectronic applications J. Phys. Chem. C 2007, 111 (32) 11921-11926
40. Zhou, H. X. Effect of mixed macromolecular crowding agents on protein folding Proteins: Struct., Funct., Bioinf. 2008, 72 (4) 1109-1113
41. Tran, D. N.; Balkus, K. J. Perspective of recent progress in immobilization of enzymes ACS Catal. 2011, 1 (8) 956-968